ID   EEP_ENTFA               Reviewed;         422 AA.
AC   Q9RPP2;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable protease eep;
DE            EC=3.4.24.-;
GN   Name=eep; OrderedLocusNames=EF_2380;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OG1X;
RX   PubMed=10498702; DOI=10.1128/jb.181.19.5915-5921.1999;
RA   An F.Y., Sulavik M.C., Clewell D.B.;
RT   "Identification and characterization of a determinant (eep) on the
RT   Enterococcus faecalis chromosome that is involved in production of the
RT   peptide sex pheromone cAD1.";
RL   J. Bacteriol. 181:5915-5921(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Involved in production of the peptide pheromone cAD1.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AF152237; AAD47948.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO82101.1; -; Genomic_DNA.
DR   RefSeq; NP_816031.1; NC_004668.1.
DR   RefSeq; WP_002359768.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q9RPP2; -.
DR   SMR; Q9RPP2; -.
DR   STRING; 226185.EF_2380; -.
DR   EnsemblBacteria; AAO82101; AAO82101; EF_2380.
DR   KEGG; efa:EF2380; -.
DR   PATRIC; fig|226185.45.peg.1158; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..422
FT                   /note="Probable protease eep"
FT                   /id="PRO_0000088423"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          179..273
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CONFLICT        114
FT                   /note="I -> V (in Ref. 1; AAD47948)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  46500 MW;  DCF96A781950FD34 CRC64;
     MKTIITFIIV FGILVLVHEF GHFYFAKRAG ILVREFAIGM GPKIFAHRGK DGTTYTIRLL
     PIGGYVRMAG MGEDMTEITP GMPLSVELNA VGNVVKINTS KKVQLPHSIP MEVIDFDLEK
     ELFIKGYVNG NEEEETVYKV DHDATIIESD GTEVRIAPLD VQFQSAKLSQ RILTNFAGPM
     NNFILGFILF TLAVFLQGGV TDLNTNQIGQ VIPNGPAAEA GLKENDKVLS INNQKIKKYE
     DFTTIVQKNP EKPLTFVVER NGKEEQLTVT PEKQKVEKQT IGKVGVYPYM KTDLPSKLMG
     GIQDTLNSTT QIFKALGSLF TGFSLNKLGG PVMMFKLSEE ASNAGVSTVV FLMAMLSMNL
     GIINLLPIPA LDGGKIVLNI IEGVRGKPIS PEKEGIITLI GFGFVMVLMV LVTWNDIQRF
     FF